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Cover Picture: Assessment of a Large Enzyme–Drug Complex by Proton‐Detected Solid‐State NMR Spectroscopy without Deuteration (Angew. Chem. Int. Ed. 17/2019)
Author(s) -
Vasa Suresh K.,
Singh Himanshu,
Grohe Kristof,
Linser Rasmus
Publication year - 2019
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201902502
Subject(s) - magic angle spinning , solid state nuclear magnetic resonance , nuclear magnetic resonance spectroscopy , spectroscopy , spinning , solid state , molecule , deuterium , chemistry , small molecule , magic angle , crystallography , materials science , nanotechnology , nuclear magnetic resonance , physics , stereochemistry , atomic physics , biochemistry , organic chemistry , quantum mechanics , polymer chemistry
Moving pictures of proteins were obtained by solid‐state NMR spectroscopy of small amounts of non‐deuterated sample by employing fast magic‐angle‐spinning rotors. From a consideration of previous approaches involving deuteration, this preview by R. Linser and co‐workers forecasts a largely facilitated sample preparation even for demanding future targets. In their Communication on page 5758 ff., they describe comprehensive insight into the structure and dynamics of a complex between a 29 kDa enzyme and a small‐molecule inhibitor.